Analytical Data
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Gene name
COL1a2
- Application
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Alternative Names
COL1a2；Collagen alpha-2(I) chain
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P08123
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Expression Region
1133-1366aa
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AA Sequence
YEVDATLKSLNNQIETLLTPEGSRKNPARTCRDLRLSHPEWSSGYYWIDP NQGCTMDAIKVYCDFSTGETCIRAQPENIPAKNWYRSSKDKKHVWLGETI NAGSQFEYNVEGVTSKEMATQLAFMRLLANYASQNITYHCKNSIAYMDEE TGNLKKAVILQGSNDVELVAEGNSRFTYTVLVDGCSKKTNEWGKTIIEYK TNKPSRLPFLDIAPLDIGGADQEFFVDIGPVCFK
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Molecular Weight
27 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
COL1A2, a gene encoding the alpha 2 chain of type I collagen, plays a crucial role in the formation of collagen fibers, which are essential for maintaining the structural integrity of various tissues, including bones, tendons, and skin. Mutations in the COL1A2 gene are associated with various connective tissue disorders, such as osteogenesis imperfecta and Ehlers-Danlos syndrome. Research involving COL1A2 recombinant proteins has gained significant attention for its potential therapeutic applications and insights into collagen-related pathologies. By producing recombinant COL1A2 proteins, scientists can study their structural and functional properties, investigate the mechanisms of collagen assembly, and explore how mutations impact collagen stability and functionality. Additionally, these recombinant proteins can be used as tools in drug development, tissue engineering, and regenerative medicine, offering possibilities for developing biomaterials that mimic native tissues or for designing targeted treatments for collagen-related diseases. Understanding COL1A2's interactions with other extracellular matrix components and its role in tissue development can lead to innovative strategies for addressing various musculoskeletal disorders, making this area of research highly relevant in biomedical science.
